NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2058895476|gb|KAG7213744|]
View 

hypothetical protein KM043_002973 [Ampulex compressa]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MH2_SMAD_1_5_9 cd10497
C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at ...
 1257-1457 1.03e-154

C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD1, SMAD5 and SMAD9 (also known as SMAD8), are receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in BMP signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


:

Pssm-ID: 199822  Cd Length: 201  Bit Score: 465.89  E-value: 1.03e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1257 YQEPPYWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNNSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 1336
Cdd:cd10497      1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1337 AECLSDSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 1416
Cdd:cd10497     81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2058895476 1417 HRQDVTSTPCWIEAHLHGPLQWLDKVLTQMGSPHNAISSVS 1457
Cdd:cd10497    161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 1013-1134 8.93e-86

N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD1, SMAD5 and SMAD9, all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


:

Pssm-ID: 199814  Cd Length: 124  Bit Score: 275.15  E-value: 8.93e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1013 SPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAVEELERALSCPGTPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 1092
Cdd:cd10490      3 SPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2058895476 1093 VWRWPDLQSHHELKPLDLCQYPFSAKQKEVCINPYHYKRVES 1134
Cdd:cd10490     83 VWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1105-1250 1.77e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.93  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1105 LKPLDL--CQYPFSAKQKEVCINPYHYKRVESPVLPPVL---------------------VPRHSEYPPgHSLLPFQ--Q 1159
Cdd:pfam03154  396 LKPLSSlsTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLtqsqslpppaashpptsglhqVPSQSPFPQ-HPFVPGGppP 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1160 IAEPTMPQnVSYSSSGfnagstGGVNPTSPMSSVGSVPSPGSTTSPNP-----QSPYGTNGLPETPPPaysppedgsqPG 1234
Cdd:pfam03154  475 ITPPSGPP-TSTSSAM------PGIQPPSSASVSSSGPVPAAVSCPLPpvqikEEALDEAEEPESPPP----------PP 537

                          170
                   ....*....|....*.
gi 2058895476 1235 QSPPPDPVPMDTTGPA 1250
Cdd:pfam03154  538 RSPSPEPTVVNTPSHA 553
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 806-906 1.94e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  806 QLLTQALKYYPSNVPWLRLMGDLNFVLGYYESAIKYYLEAIMVASDFFSqpvprtqiddlVYRRMIKCCAHLQCYTQAAV 885
Cdd:COG2956    165 EALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP-----------ALPRLAELYEKLGDPEEALE 233

                           90       100
                   ....*....|....*....|.
gi 2058895476  886 LCQFLEEVDYSLAFKMAASDL 906
Cdd:COG2956    234 LLRKALELDPSDDLLLALADL 254
 
Name Accession Description Interval E-value
MH2_SMAD_1_5_9 cd10497
C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at ...
 1257-1457 1.03e-154

C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD1, SMAD5 and SMAD9 (also known as SMAD8), are receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in BMP signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199822  Cd Length: 201  Bit Score: 465.89  E-value: 1.03e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1257 YQEPPYWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNNSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 1336
Cdd:cd10497      1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1337 AECLSDSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 1416
Cdd:cd10497     81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2058895476 1417 HRQDVTSTPCWIEAHLHGPLQWLDKVLTQMGSPHNAISSVS 1457
Cdd:cd10497    161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
DWB smart00524
Domain B in dwarfin family proteins;
1262-1433 1.99e-95

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 304.23  E-value: 1.99e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  1262 YWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNnSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLS 1341
Cdd:smart00524    1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSD-GNRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  1342 DSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDV 1421
Cdd:smart00524   80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                           170
                    ....*....|..
gi 2058895476  1422 TSTPCWIEAHLH 1433
Cdd:smart00524  160 TSTPCWIEVHLN 171
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 1261-1433 2.05e-94

MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD related proteins such as Smads. This domain is separated from the MH1 domain by a non-conserved linker region. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers. Unlike MH1, MH2 does not bind DNA. The well-studied MH2 domain of Smad4 is composed of five alpha helices and three loops enclosing a beta sandwich. Smads are involved in the propagation of TGF-beta signals by direct association with the TGF-beta receptor kinase which phosphorylates the last two Ser of a conserved 'SSXS' motif located at the C-terminus of MH2.


Pssm-ID: 460834  Cd Length: 172  Bit Score: 301.46  E-value: 2.05e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1261 PYWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNNsDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECL 1340
Cdd:pfam03166    1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1341 SDSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQD 1420
Cdd:pfam03166   80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                          170
                   ....*....|...
gi 2058895476 1421 VTSTPCWIEAHLH 1433
Cdd:pfam03166  160 ITSTPCWIEIHLH 172
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 1013-1134 8.93e-86

N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD1, SMAD5 and SMAD9, all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199814  Cd Length: 124  Bit Score: 275.15  E-value: 8.93e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1013 SPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAVEELERALSCPGTPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 1092
Cdd:cd10490      3 SPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2058895476 1093 VWRWPDLQSHHELKPLDLCQYPFSAKQKEVCINPYHYKRVES 1134
Cdd:cd10490     83 VWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
DWA smart00523
Domain A in dwarfin family proteins;
1027-1136 1.18e-56

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 191.44  E-value: 1.18e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  1027 EEEKWAEKAVDSLVKKLKKRKgaVEELERALSCPGT-PSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 1105
Cdd:smart00523    1 VEEKWAKKATESLLKKLKKKQ--LEELLQAVESKGGpPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                            90       100       110
                    ....*....|....*....|....*....|.
gi 2058895476  1106 KPLDLCQYPFSAKQKEVCINPYHYKRVESPV 1136
Cdd:smart00523   79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 1032-1133 3.31e-54

MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related proteins such as Smads. This domain is separated from the MH2 domain by a non-conserved linker region. The crystal structure of the MH1 domain shows that a highly conserved 11 residue beta hairpin is used to bind the DNA consensus sequence GNCN in the major groove, shown to be vital for the transcriptional activation of target genes. Not all examples of MH1 can bind to DNA however. Smad2 cannot bind DNA and has a large insertion within the hairpin that presumably abolishes DNA binding. A basic helix (H2) in MH1 with the nuclear localization signal KKLKK has been shown to be essential for Smad3 nuclear import. Smads also use the MH1 domain to interact with transcription factors such as Jun, TFE3, Sp1, and Runx.


Pssm-ID: 460833  Cd Length: 103  Bit Score: 184.11  E-value: 3.31e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1032 AEKAVDSLVKKLKKRKGAVEELERALSCPG-TPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDL 1110
Cdd:pfam03165    1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                           90       100
                   ....*....|....*....|...
gi 2058895476 1111 CQYPFSAKQKEVCINPYHYKRVE 1133
Cdd:pfam03165   81 CETAFESKKDEVCINPYHYSRVE 103
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1105-1250 1.77e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.93  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1105 LKPLDL--CQYPFSAKQKEVCINPYHYKRVESPVLPPVL---------------------VPRHSEYPPgHSLLPFQ--Q 1159
Cdd:pfam03154  396 LKPLSSlsTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLtqsqslpppaashpptsglhqVPSQSPFPQ-HPFVPGGppP 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1160 IAEPTMPQnVSYSSSGfnagstGGVNPTSPMSSVGSVPSPGSTTSPNP-----QSPYGTNGLPETPPPaysppedgsqPG 1234
Cdd:pfam03154  475 ITPPSGPP-TSTSSAM------PGIQPPSSASVSSSGPVPAAVSCPLPpvqikEEALDEAEEPESPPP----------PP 537

                          170
                   ....*....|....*.
gi 2058895476 1235 QSPPPDPVPMDTTGPA 1250
Cdd:pfam03154  538 RSPSPEPTVVNTPSHA 553
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1171-1254 1.03e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1171 YSSSGFNAGSTGGVNPTSPMSSVGSVPSPGSTTSPNPQSPygtngLPETPPPAYSPPEDGSQPgqSPPPDPVPMDTTGPA 1250
Cdd:PHA03247   390 HAATPFARGPGGDDQTRPAAPVPASVPTPAPTPVPASAPP-----PPATPLPSAEPGSDDGPA--PPPERQPPAPATEPA 462


                   ....
gi 2058895476 1251 EVAP 1254
Cdd:PHA03247   463 PDDP 466
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 806-906 1.94e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  806 QLLTQALKYYPSNVPWLRLMGDLNFVLGYYESAIKYYLEAIMVASDFFSqpvprtqiddlVYRRMIKCCAHLQCYTQAAV 885
Cdd:COG2956    165 EALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP-----------ALPRLAELYEKLGDPEEALE 233

                           90       100
                   ....*....|....*....|.
gi 2058895476  886 LCQFLEEVDYSLAFKMAASDL 906
Cdd:COG2956    234 LLRKALELDPSDDLLLALADL 254
 
Name Accession Description Interval E-value
MH2_SMAD_1_5_9 cd10497
C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at ...
 1257-1457 1.03e-154

C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD1, SMAD5 and SMAD9 (also known as SMAD8), are receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in BMP signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199822  Cd Length: 201  Bit Score: 465.89  E-value: 1.03e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1257 YQEPPYWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNNSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 1336
Cdd:cd10497      1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1337 AECLSDSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 1416
Cdd:cd10497     81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2058895476 1417 HRQDVTSTPCWIEAHLHGPLQWLDKVLTQMGSPHNAISSVS 1457
Cdd:cd10497    161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
MH2_R-SMAD cd10495
C-terminal Mad Homology 2 (MH2) domain in receptor regulated SMADs; The MH2 domain is located ...
 1263-1444 1.44e-132

C-terminal Mad Homology 2 (MH2) domain in receptor regulated SMADs; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. Receptor regulated SMADs (R-SMADs) include SMAD1, SMAD2, SMAD3, SMAD5 and SMAD9. SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta. SMAD5 is involved in BMP signal modulation, possibly playing a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 (also known as SMAD8) can mediate the differentiation of mesenchymal stem cells into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199820  Cd Length: 182  Bit Score: 405.99  E-value: 1.44e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1263 WASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNNSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSD 1342
Cdd:cd10495      1 WCSISYYELNSRVGEQFKASNPSIIVDGFTDPSNNSDRFCLGLLSNVNRNATIENTRRHIGRGVHLFYVGGEVYAECLSD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1343 SAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVT 1422
Cdd:cd10495     81 SAIFVQSRNCNLRHGFHPATVCKIPPGCSLKIFNNQSFAQLLEQSVNRGFEAVYELTKMCTIRISFVKGWGAEYHRQDVT 160

                          170       180
                   ....*....|....*....|..
gi 2058895476 1423 STPCWIEAHLHGPLQWLDKVLT 1444
Cdd:cd10495    161 STPCWIEIHLHGPLQWLDKVLT 182
MH2_SMAD_2_3 cd10985
C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3; The MH2 domain is located at the ...
 1255-1446 4.50e-122

C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. SMAD2 and SMAD3 are receptor regulated SMADs (R-SMADs). SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta.


Pssm-ID: 199826  Cd Length: 191  Bit Score: 378.12  E-value: 4.50e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1255 VCYQEPPYWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNnSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGE 1334
Cdd:cd10985      1 VTYCEPAFWCSISYYEMNTRVGETFHASQPSLTVDGFTDPSN-SERFCLGLLSNVNRNPQVELTRRHIGKGVRLYYIGGE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1335 VYAECLSDSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGA 1414
Cdd:cd10985     80 VFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLSQSVNQGFEAVYQLTRMCTIRMSFVKGWGA 159

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2058895476 1415 EYHRQDVTSTPCWIEAHLHGPLQWLDKVLTQM 1446
Cdd:cd10985    160 EYRRQTVTSTPCWIELHLNGPLQWLDRVLTQM 191
MH2 cd00050
C-terminal Mad Homology 2 (MH2) domain; The MH2 domain is found in the SMAD (small mothers ...
 1263-1433 2.33e-110

C-terminal Mad Homology 2 (MH2) domain; The MH2 domain is found in the SMAD (small mothers against decapentaplegic) family of proteins and is responsible for type I receptor interactions, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain which prevents it from forming a complex with SMAD4. The MH2 domain is multifunctional and provides SMADs with their specificity and selectivity, as well as transcriptional activity. Several transcriptional co-activators and repressors have also been reported to regulate SMAD signaling by interacting with the MH2 domain. Mutations in the MH2 domains of SMAD2 and especially SMAD4 have been detected in colorectal and other human cancers.


Pssm-ID: 199819  Cd Length: 170  Bit Score: 345.36  E-value: 2.33e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1263 WASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNnSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSD 1342
Cdd:cd00050      1 WCSIAYYELNTRVGELFHVYSPSVAVDGFTDPSN-GDRFCLGQLSNVNRNETIERTRRHIGKGVHLYYVGGEVWAECLSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1343 SAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVT 1422
Cdd:cd00050     80 HAIFVQSRNLDYPHGRHPLTVCKIPPGCSIKVFDNQEFAQLLHQSVNTGFEGVYELTKMCTIRMSFVKGWGPEYHRQDIT 159

                          170
                   ....*....|.
gi 2058895476 1423 STPCWIEAHLH 1433
Cdd:cd00050    160 STPCWIEIHLH 170
DWB smart00524
Domain B in dwarfin family proteins;
1262-1433 1.99e-95

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 304.23  E-value: 1.99e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  1262 YWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNnSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLS 1341
Cdd:smart00524    1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSD-GNRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  1342 DSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDV 1421
Cdd:smart00524   80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                           170
                    ....*....|..
gi 2058895476  1422 TSTPCWIEAHLH 1433
Cdd:smart00524  160 TSTPCWIEVHLN 171
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 1261-1433 2.05e-94

MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD related proteins such as Smads. This domain is separated from the MH1 domain by a non-conserved linker region. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers. Unlike MH1, MH2 does not bind DNA. The well-studied MH2 domain of Smad4 is composed of five alpha helices and three loops enclosing a beta sandwich. Smads are involved in the propagation of TGF-beta signals by direct association with the TGF-beta receptor kinase which phosphorylates the last two Ser of a conserved 'SSXS' motif located at the C-terminus of MH2.


Pssm-ID: 460834  Cd Length: 172  Bit Score: 301.46  E-value: 2.05e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1261 PYWASIAYYELNCRVGEVFHCQTHSVIVDGFTNPSNNsDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECL 1340
Cdd:pfam03166    1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1341 SDSAIFVQSRNCNHHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQD 1420
Cdd:pfam03166   80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                          170
                   ....*....|...
gi 2058895476 1421 VTSTPCWIEAHLH 1433
Cdd:pfam03166  160 ITSTPCWIEIHLH 172
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 1013-1134 8.93e-86

N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD1, SMAD5 and SMAD9, all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199814  Cd Length: 124  Bit Score: 275.15  E-value: 8.93e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1013 SPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAVEELERALSCPGTPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 1092
Cdd:cd10490      3 SPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2058895476 1093 VWRWPDLQSHHELKPLDLCQYPFSAKQKEVCINPYHYKRVES 1134
Cdd:cd10490     83 VWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
MH1_R-SMAD cd10488
N-terminal Mad Homology 1 (MH1) domain of receptor regulated SMADs; The MH1 is a small ...
 1014-1134 1.33e-70

N-terminal Mad Homology 1 (MH1) domain of receptor regulated SMADs; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. It binds to the major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in all receptor regulated SMADs (R-SMADs) including SMAD1, SMAD2, SMAD3, SMAD5 and SMAD9. SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta. SMAD4, a common mediator SMAD (co-SMAD) binds R-SMADs, forming an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation, possibly playing a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 (also known as SMAD8) can mediate the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway


Pssm-ID: 199812  Cd Length: 123  Bit Score: 231.69  E-value: 1.33e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1014 PAVKKLLGWKQG---DEEEKWAEKAVDSLVKKLKKrKGAVEELERALSCPGTPSKCVTIPRSLDGRLQVSHRKGLPHVIY 1090
Cdd:cd10488      1 PIVKRLLGWKKGeqnGEEEKWAEKAVKSLVKKLKK-KGQLEELEKAISTQNVNTRCVTIPRSLDGRLQVSHRKGLPHVIY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2058895476 1091 CRVWRWPDLQSHHELKPLDLCQYPFSAKQKEVCINPYHYKRVES 1134
Cdd:cd10488     80 CRLWRWPDLQSHHELKPLELCEFAFNMKKEEVCINPYHYKRVET 123
MH1_SMAD_2_3 cd10491
N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3; The MH1 is a small DNA-binding ...
 1013-1134 4.05e-68

N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 is found in SMAD2 as well as SMAD3. SMAD2 mediates the signal of the transforming growth factor (TGF)-beta, and thereby regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. It plays a role in the transmission of extracellular signals from ligands of the TGF-beta superfamily growth factors into the cell nucleus. SMAD3 modulates signals of activin and TGF-beta. It binds SMAD4, enabling its transmigration into the nucleus where it forms complexes with other proteins and acts as a transcription factor. Increased SMAD3 activity has been implicated in the pathogenesis of scleroderma.


Pssm-ID: 199815  Cd Length: 124  Bit Score: 224.72  E-value: 4.05e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1013 SPAVKKLLGWKQG--DEEEKWAEKAVDSLVKKLKKrKGAVEELERALSCPGTPSKCVTIPRSLDGRLQVSHRKGLPHVIY 1090
Cdd:cd10491      2 PPVVKRLLGWKKGenGQEEKWSEKAVKSLVKKLKK-TGGLDELEKAITTQNSNTKCITIPRSLDGRLQVSHRKGLPHVIY 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2058895476 1091 CRVWRWPDLQSHHELKPLDLCQYPFSAKQKEVCINPYHYKRVES 1134
Cdd:cd10491     81 CRLWRWPDLQSHHELRAIETCEYAFNLKKDEVCVNPYHYQRVET 124
MH1 cd00049
N-terminal Mad Homology 1 (MH1) domain; The MH1 is a small DNA-binding domain present in SMAD ...
 1014-1134 2.50e-67

N-terminal Mad Homology 1 (MH1) domain; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. Receptor-regulated SMAD proteins (R-SMADs, including SMAD1, SMAD2, SMAD3, SMAD5, and SMAD9) are activated by phosphorylation by transforming growth factor (TGF)-beta type I receptors. The active R-SMAD associates with a common mediator SMAD (Co-SMAD or SMAD4) and other cofactors, which together translocate to the nucleus to regulate gene expression. The inhibitory or antagonistic SMADs (I-SMADs, including SMAD6 and SMAD7) negatively regulate TGF-beta signaling by competing with R-SMADs for type I receptor or Co-SMADs. MH1 domains of R-SMAD and SMAD4 contain a nuclear localization signal as well as DNA-binding activity. The activated R-SMAD/SMAD4 complex then binds with very low affinity to a DNA sequence CAGAC called SMAD-binding element (SBE) via the MH1 domain.


Pssm-ID: 199811  Cd Length: 121  Bit Score: 222.46  E-value: 2.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1014 PAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKgAVEELERALSCPG-TPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 1092
Cdd:cd00049      1 PIVKRLLGWKQGGEEEKWAKKAVKSLVKKLKEKK-QLDSLEKAITTQGgVPSKCVTIPRSLDGRLQVAHRKGLPHVIYCR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2058895476 1093 VWRWPDLQSHHELKPLDLCQYPFSAKQKEVCINPYHYKRVES 1134
Cdd:cd00049     80 LWRWPDLHSHHELKALELCQFAFNMKKDEVCVNPYHYQRVES 121
DWA smart00523
Domain A in dwarfin family proteins;
1027-1136 1.18e-56

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 191.44  E-value: 1.18e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  1027 EEEKWAEKAVDSLVKKLKKRKgaVEELERALSCPGT-PSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 1105
Cdd:smart00523    1 VEEKWAKKATESLLKKLKKKQ--LEELLQAVESKGGpPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                            90       100       110
                    ....*....|....*....|....*....|.
gi 2058895476  1106 KPLDLCQYPFSAKQKEVCINPYHYKRVESPV 1136
Cdd:smart00523   79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH2_SMAD_4 cd10498
C-terminal Mad Homology 2 (MH2) domain in SMAD4; The MH2 domain is located at the C-terminus ...
 1260-1443 2.20e-56

C-terminal Mad Homology 2 (MH2) domain in SMAD4; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. SMAD4, which belongs to the Dwarfin family of proteins, is involved in many cell functions such as differentiation, apoptosis, gastrulation, embryonic development and the cell cycle. SMAD4 binds receptor regulated SMADs (R-SMADs) such as SMAD1 or SMAD2, and forms an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD4 is often mutated in several cancers, such as multiploid colorectal cancer, cervical cancer and pancreatic carcinoma, as well as in juvenile polyposis syndrome.


Pssm-ID: 199823  Cd Length: 222  Bit Score: 195.00  E-value: 2.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1260 PPYWASIAYYELNCRVGEVFHC--QTHSVIVDGFTNPSNnSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVG-GEVY 1336
Cdd:cd10498      1 PEYWCSIAYFELDTQVGETFKVpsSCPTVTVDGYVDPSG-GNRFCLGQLSNVHRTEASERARLHIGKGVQLDCKGeGDVW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1337 AECLSDSAIFVQSRNCNHHHGFHP-STVCKIPPGCSLKIFN-NQEFAQLLSQSVNHGFEA-------------------- 1394
Cdd:cd10498     80 LRCLSDHSVFVQSYYLDREAGRAPgDAVHKIYPSAYIKVFDlRQCHRQMQQQAATAQAAAaaqaaavagnipgpgsvggi 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2058895476 1395 -------------VYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEAHLHGPLQWLDKVL 1443
Cdd:cd10498    160 apaislsaaagigVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVL 221
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 1032-1133 3.31e-54

MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related proteins such as Smads. This domain is separated from the MH2 domain by a non-conserved linker region. The crystal structure of the MH1 domain shows that a highly conserved 11 residue beta hairpin is used to bind the DNA consensus sequence GNCN in the major groove, shown to be vital for the transcriptional activation of target genes. Not all examples of MH1 can bind to DNA however. Smad2 cannot bind DNA and has a large insertion within the hairpin that presumably abolishes DNA binding. A basic helix (H2) in MH1 with the nuclear localization signal KKLKK has been shown to be essential for Smad3 nuclear import. Smads also use the MH1 domain to interact with transcription factors such as Jun, TFE3, Sp1, and Runx.


Pssm-ID: 460833  Cd Length: 103  Bit Score: 184.11  E-value: 3.31e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1032 AEKAVDSLVKKLKKRKGAVEELERALSCPG-TPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDL 1110
Cdd:pfam03165    1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                           90       100
                   ....*....|....*....|...
gi 2058895476 1111 CQYPFSAKQKEVCINPYHYKRVE 1133
Cdd:pfam03165   81 CETAFESKKDEVCINPYHYSRVE 103
MH1_SMAD_4 cd10492
N-terminal Mad Homology 1 (MH1) domain in SMAD4; The MH1 is a small DNA-binding domain present ...
 1016-1134 5.74e-45

N-terminal Mad Homology 1 (MH1) domain in SMAD4; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD4, a common mediator SMAD (co-SMAD), which belongs to the Dwarfin family of proteins and is involved in many cell functions such as differentiation, apoptosis, gastrulation, embryonic development and cell cycle. SMAD4 binds receptor regulated SMADs (R-SMADs) such as SMAD1 or SMAD2, and forms an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD4 is often mutated in several cancers, such as multiploid colorectal cancer and pancreatic carcinoma, as well as in juvenile polyposis syndrome (JPS).


Pssm-ID: 199816  Cd Length: 125  Bit Score: 158.38  E-value: 5.74e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1016 VKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAVEELERALSCPGT-PSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVW 1094
Cdd:cd10492      7 VHSLMCHRQGGESESFAKRAIESLVKKLKDKRDELDSLITAITSNGAhPSKCVTIQRTLDGRLQVAGRKGFPHVIYARIW 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2058895476 1095 RWPDLQShHELKPLDLCQYPFSAKQKEVCINPYHYKRVES 1134
Cdd:cd10492     87 RWPDLHK-NELKHVKFCQYAFDLKCDSVCVNPYHYERVVS 125
MH2_I-SMAD cd10496
C-terminal Mad Homology 2 (MH2) domain in Inhibitory SMADs; The MH2 domain is located at the ...
 1263-1432 1.17e-34

C-terminal Mad Homology 2 (MH2) domain in Inhibitory SMADs; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD6 and SMAD7 are inhibitory SMADs (I-SMADs) that function as negative regulators of signaling mediated by the TGF-beta superfamily. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling, while SMAD7 enhances muscle differentiation and is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199821  Cd Length: 165  Bit Score: 130.55  E-value: 1.17e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1263 WASIAYYELNCRVGEVFHCQTHSVIVdgFTNpSNNSDRFCLGQL-SNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLS 1341
Cdd:cd10496      1 WCTIAYWELRERVGRLYPVKQPAVNI--FDD-LPKGDGFCLGALnRQGNASEAVARVRSKIGLGVTLSREPDGVWIYNRS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1342 DSAIFVQSRNCNHHHGFHPsTVCKIPPGCSLKIFNNQEFAQLlsQSVNHGFEAVYELTKMcTIRMSFVKGWGAEYHRQDV 1421
Cdd:cd10496     78 EYPIFVNSPTLDSPPSRNL-LVTKVPPGYSLKVFDYERAALL--QRRDDHFSPQGPVDPN-SVRISFVKGWGPNYSRQFI 153

                          170
                   ....*....|.
gi 2058895476 1422 TSTPCWIEAHL 1432
Cdd:cd10496    154 TSCPCWLEILL 164
MH2_SMAD_6 cd10499
C-terminal Mad Homology 2 (MH2) domain in SMAD6; The MH2 domain is located at the C-terminus ...
 1259-1429 6.69e-27

C-terminal Mad Homology 2 (MH2) domain in SMAD6; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD6, an inhibitory or antagonistic SMAD (I-SMAD), acts as a negative regulator of signaling mediated by the TGF-beta superfamily of ligands, by competing with SMAD4 and preventing the transcription of SMAD4's gene products. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling. SMAD6 and SMAD7 act as critical mediators for effective TGF-beta I-mediated suppression of Interleukin-1/Toll-like receptor (IL-1R/TLR) signaling through simultaneous binding to Pellino-1, an adaptor protein of interleukin-1 receptor associated kinase 1 (IRAK1), via their MH2 domains.


Pssm-ID: 199824  Cd Length: 174  Bit Score: 108.76  E-value: 6.69e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1259 EPPYWASIAYYELNCRVGEVFHCQTHSVIVdgFTN-PsnNSDRFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYA 1337
Cdd:cd10499      6 KRSHWCSVAYWEHRTRVGRLYAVYDQSVSI--FYDlP--QGSGFCLGQLNLEQRSESVRRTRSKIGYGILLSKEPDGVWA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1338 ECLSDSAIFVQSRNCNHHHGfHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTkmcTIRMSFVKGWGAEYH 1417
Cdd:cd10499     82 YNRSEHPIFVNSPTLDIPGS-RTLVVRKVPPGYSIKVFDYERSCLLQHTAEPELADGPYDPN---SVRISFAKGWGPCYS 157

                          170
                   ....*....|..
gi 2058895476 1418 RQDVTSTPCWIE 1429
Cdd:cd10499    158 RQFITSCPCWLE 169
MH1_SMAD_6_7 cd10489
N-terminal Mad Homology 1 (MH1) domain in SMAD6 and SMAD7; The MH1 is a small DNA-binding ...
 1034-1135 3.74e-19

N-terminal Mad Homology 1 (MH1) domain in SMAD6 and SMAD7; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD6 and SMAD7, both inhibitory SMADs (I-SMADs) and negative regulators of signaling mediated by TGF-beta superfamily. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling while SMAD7 enhances muscle differentiation and is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199813  Cd Length: 119  Bit Score: 84.74  E-value: 3.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1034 KAVDSLVKKLKKRKgaVEELERAL-SCPGTPSKCVTIPRSLdgrlqVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDLCQ 1112
Cdd:cd10489     25 AAFHALLKRLKEKQ--LELLLQAVeSRGGDYLACVLLPRRD-----PRSMPQDPHVLCCQLFRWPDLRHSSELKRLPTCE 97

                           90       100
                   ....*....|....*....|....
gi 2058895476 1113 ypfSAKQKE-VCINPYHYKRVESP 1135
Cdd:cd10489     98 ---SAKDPVyVCCNPYHWSRLCRP 118
MH1_SMAD_6 cd10493
N-terminal Mad Homology 1 (MH1) domain in SMAD6; The MH1 is a small DNA-binding domain present ...
 1025-1136 5.08e-19

N-terminal Mad Homology 1 (MH1) domain in SMAD6; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD6, an inhibitory SMAD (I-SMAD) or antagonistic SMAD, which acts as a negative regulator of signaling mediated by TGF-beta superfamily ligands, by competing with SMAD4 and preventing the transcription of SMAD4's gene products. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling.


Pssm-ID: 199817  Cd Length: 113  Bit Score: 84.05  E-value: 5.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1025 GDEEEKwaeKAVDSLVKKLKKRkgAVEELERAL-SCPGTPSKCVTIPRSldgRLQVSHRKGLPHVIYCRVWRWPDLQSHH 1103
Cdd:cd10493      9 LEQELK---SVTYALLKRLKER--SLDVLLEAVeSRGGLPSGCVMVPRT---ELRLGGRRVPPQLLLCRLFRWPDLQHPA 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2058895476 1104 ELKPLDLCQYPFSAKQKEVCINPYHYKRVESPV 1136
Cdd:cd10493     81 QLKALCHCQSFGAQDGPTVCCNPYHYSRLCGPE 113
MH2_SMAD_7 cd10500
C-terminal Mad Homology 2 (MH2) domain in SMAD7; The MH2 domain is located at the C-terminus ...
 1259-1429 8.08e-19

C-terminal Mad Homology 2 (MH2) domain in SMAD7; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD7, an inhibitory or antagonistic SMAD (I-SMAD), acts as a negative regulator of signaling mediated by the TGF-beta superfamily of ligands, by blocking TGF-beta type 1 and activin association with the receptor as well as access to SMAD2. SMAD7 enhances muscle differentiation, playing pivotal roles in embryonic development and adult homoeostasis. SMAD7 and SMAD6 act as critical mediators for effective TGF-beta I-mediated suppression of Interleukin-1/Toll-like receptor (IL-1R/TLR) signaling through simultaneous binding to Pellino-1, an adaptor protein of interleukin-1 receptor associated kinase 1(IRAK1), via their MH2 domains. Altered expression of SMAD7 is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199825  Cd Length: 171  Bit Score: 85.48  E-value: 8.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1259 EPPYWASIAYYELNCRVGEVFHCQTHSVivDGFTN-PSNNSdrFCLGQLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYA 1337
Cdd:cd10500      4 DQSHWCVVAYWEEKTRVGRLYSVQEPSL--DIFYDlPQGNG--FCLGQLNSDNKSQLVQKVRSKIGYGIQLTREVDGVWV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1338 ECLSDSAIFVQSRNCNHHHGfHPSTVCKIPPGCSLKIFNNQEfAQLLSQSVNHGFeaVYELTKMCTIRMSFVKGWGAEYH 1417
Cdd:cd10500     80 YNRSSYPIFIKSATLDNPDS-RTLLVHKVFPGFSIKAFDYEK-AYSLQRPNDHEF--MQQPWTGFTVQISFVKGWGQCYT 155

                          170
                   ....*....|..
gi 2058895476 1418 RQDVTSTPCWIE 1429
Cdd:cd10500    156 RQFISSCPCWLE 167
MH1_SMAD_7 cd10494
N-terminal Mad Homology 1 (MH1) domain in SMAD7; The MH1 is a small DNA-binding domain present ...
 1038-1135 7.06e-13

N-terminal Mad Homology 1 (MH1) domain in SMAD7; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins. It binds to the major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD7, an inhibitory SMAD (I-SMAD) or antagonistic SMAD, which acts as a negative regulator of signaling mediated by TGF-beta superfamily ligands, by blocking TGF-beta type 1 and activin association with the receptor as well as access to SMAD2. SMAD7 enhances muscle differentiation, playing pivotal roles in embryonic development and adult homoeostasis. Altered expression of SMAD7 is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199818  Cd Length: 123  Bit Score: 66.82  E-value: 7.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1038 SLVKKLKKRKgaVEELERALSCPG-TPSKCVTIPRSLDGRLQvSHRKGLPhVIYCRVWRWPDLQSHHELKPLDLCQYPFS 1116
Cdd:cd10494     26 SVLKKLKERQ--LEGLLQAVESRGgARTPCLLLPARLDARLG-QQSYSLP-LLLCKVFRWPDLRHSSEVKRLSCCESYGK 101

                           90       100
                   ....*....|....*....|..
gi 2058895476 1117 AKQKEVCINPYHYKR---VESP 1135
Cdd:cd10494    102 INPELVCCNPHHLSRlceLESP 123
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1105-1250 1.77e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.93  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1105 LKPLDL--CQYPFSAKQKEVCINPYHYKRVESPVLPPVL---------------------VPRHSEYPPgHSLLPFQ--Q 1159
Cdd:pfam03154  396 LKPLSSlsTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLtqsqslpppaashpptsglhqVPSQSPFPQ-HPFVPGGppP 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1160 IAEPTMPQnVSYSSSGfnagstGGVNPTSPMSSVGSVPSPGSTTSPNP-----QSPYGTNGLPETPPPaysppedgsqPG 1234
Cdd:pfam03154  475 ITPPSGPP-TSTSSAM------PGIQPPSSASVSSSGPVPAAVSCPLPpvqikEEALDEAEEPESPPP----------PP 537

                          170
                   ....*....|....*.
gi 2058895476 1235 QSPPPDPVPMDTTGPA 1250
Cdd:pfam03154  538 RSPSPEPTVVNTPSHA 553
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1135-1272 4.09e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 54.77  E-value: 4.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1135 PVLPPVLvprHSEYPP-GHSLlpfqQIAEPTMPQNVSysSSGFnagstggvnPTSPMSSVGSVPSPgsttsPNPQSPYGT 1213
Cdd:pfam03154  265 PLPQPSL---HGQMPPmPHSL----QTGPSHMQHPVP--PQPF---------PLTPQSSQSQVPPG-----PSPAAPGQS 321

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2058895476 1214 NGLPETPPPAYSPPEdGSQPGQSP-PPDPVPMDTTGPAEVAPV-------CYQEPPYWASIAYYELN 1272
Cdd:pfam03154  322 QQRIHTPPSQSQLQS-QQPPREQPlPPAPLSMPHIKPPPTTPIpqlpnpqSHKHPPHLSGPSPFQMN 387
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1171-1254 1.03e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1171 YSSSGFNAGSTGGVNPTSPMSSVGSVPSPGSTTSPNPQSPygtngLPETPPPAYSPPEDGSQPgqSPPPDPVPMDTTGPA 1250
Cdd:PHA03247   390 HAATPFARGPGGDDQTRPAAPVPASVPTPAPTPVPASAPP-----PPATPLPSAEPGSDDGPA--PPPERQPPAPATEPA 462


                   ....
gi 2058895476 1251 EVAP 1254
Cdd:PHA03247   463 PDDP 466
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1138-1261 2.46e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.46  E-value: 2.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1138 PPVLVP------RH--SEYPPGHSLLP-FQQI-AEPTMPQNVSYSSSgfnAGSTGGVNPtsPMSSVGSVPSpgstTSPNP 1207
Cdd:pfam03154  393 PPALKPlsslstHHppSAHPPPLQLMPqSQQLpPPPAQPPVLTQSQS---LPPPAASHP--PTSGLHQVPS----QSPFP 463

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2058895476 1208 QSPYGTNGLPE-----TPPPAYSPPEDGSQPGQSPPPD---PVPMDTTGPaeVAPVCYQEPP 1261
Cdd:pfam03154  464 QHPFVPGGPPPitppsGPPTSTSSAMPGIQPPSSASVSssgPVPAAVSCP--LPPVQIKEEA 523
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 1160-1261 2.99e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.19  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1160 IAEPTMPQNVSYSSSGfNAGSTGGVNPTSPmssvgsvPSPGSTTSPNPQSPygtngLPETPPPAYSPPEDGSQPgqSPPP 1239
Cdd:PRK14950   360 LVPVPAPQPAKPTAAA-PSPVRPTPAPSTR-------PKAAAAANIPPKEP-----VRETATPPPVPPRPVAPP--VPHT 424

                           90       100
                   ....*....|....*....|....*
gi 2058895476 1240 DPVPMDTTG---PAEVAPVCYQEPP 1261
Cdd:PRK14950   425 PESAPKLTRaaiPVDEKPKYTPPAP 449
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1135-1261 3.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1135 PVLPPVLVP-RHSEYPPGHSllPFQQIAEPTMPQNVSYS-SSGFNAGST---GGVNPTSPMSSVGSVPSPGSTTSPNPQS 1209
Cdd:PHA03247  2804 PADPPAAVLaPAAALPPAAS--PAGPLPPPTSAQPTAPPpPPGPPPPSLplgGSVAPGGDVRRRPPSRSPAAKPAAPARP 2881

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2058895476 1210 PYGTNGLPETPPPAYSPPEDGSQPGQSPPPDPVPMDTTGPAEVAPVCYQEPP 1261
Cdd:PHA03247  2882 PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP 2933
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 806-906 1.94e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476  806 QLLTQALKYYPSNVPWLRLMGDLNFVLGYYESAIKYYLEAIMVASDFFSqpvprtqiddlVYRRMIKCCAHLQCYTQAAV 885
Cdd:COG2956    165 EALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP-----------ALPRLAELYEKLGDPEEALE 233

                           90       100
                   ....*....|....*....|.
gi 2058895476  886 LCQFLEEVDYSLAFKMAASDL 906
Cdd:COG2956    234 LLRKALELDPSDDLLLALADL 254
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1179-1260 2.58e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.07  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1179 GSTGGVNPTSPMSSvGSVPSPGSTTSPNPQSPYGTNGLPETP--PPAYSPPEDGSQPGQSPPPDPVPM--DTTGPAEVAP 1254
Cdd:PRK14971   371 GGRGPKQHIKPVFT-QPAAAPQPSAAAAASPSPSQSSAAAQPsaPQSATQPAGTPPTVSVDPPAAVPVnpPSTAPQAVRP 449


                   ....*.
gi 2058895476 1255 VCYQEP 1260
Cdd:PRK14971   450 AQFKEE 455
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1154-1261 4.69e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058895476 1154 LLPFQQIAEPTMPQNVSYSSSGFNAGSTGGVNPTSPMSSVGSVPSPGSttspnPQSPYGTNGLPETPPPAYSPPEDGSQP 1233
Cdd:PRK07764   363 LLPSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAP-----APAAAAPAAAAAPAPAAAPQPAPAPAP 437

                           90       100
                   ....*....|....*....|....*...
gi 2058895476 1234 GQSPPPDPVPMDTTGPAEVAPVCYQEPP 1261
Cdd:PRK07764   438 APAPPSPAGNAPAGGAPSPPPAAAPSAQ 465
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH